Iron in PDB 2euo: Cytochrome C Peroxidase (Ccp) in Complex with 1-Methyl-1- Lambda-5-Pyridin-3-Yl-Amine

All present enzymatic activity of Cytochrome C Peroxidase (Ccp) in Complex with 1-Methyl-1- Lambda-5-Pyridin-3-Yl-Amine:
1.11.1.5;

The structure of Cytochrome C Peroxidase (Ccp) in Complex with 1-Methyl-1- Lambda-5-Pyridin-3-Yl-Amine, PDB code: 2euo was solved by R.Brenk, S.W.Vetter, S.E.Boyce, D.B.Goodin, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.490, 73.570, 104.610, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 18.1

The binding sites of Iron atom in the Cytochrome C Peroxidase (Ccp) in Complex with 1-Methyl-1- Lambda-5-Pyridin-3-Yl-Amine (pdb code 2euo). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Cytochrome C Peroxidase (Ccp) in Complex with 1-Methyl-1- Lambda-5-Pyridin-3-Yl-Amine, PDB code: 2euo:

Iron binding site 1 out of 1 in the Cytochrome C Peroxidase (Ccp) in Complex with 1-Methyl-1- Lambda-5-Pyridin-3-Yl-Amine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C Peroxidase (Ccp) in Complex with 1-Methyl-1- Lambda-5-Pyridin-3-Yl-Amine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe295 b:10.5 occ:1.00 FE A:HEM295 0.0 10.5 1.0 NC A:HEM295 2.0 15.6 1.0 NA A:HEM295 2.0 15.6 1.0 ND A:HEM295 2.0 15.6 1.0 NE2 A:HIS175 2.0 11.8 1.0 NB A:HEM295 2.0 15.6 1.0 O A:HOH641 2.2 20.9 1.0 CD2 A:HIS175 3.0 10.3 1.0 C1C A:HEM295 3.0 9.3 1.0 C4C A:HEM295 3.0 8.4 1.0 CE1 A:HIS175 3.0 10.1 1.0 C4D A:HEM295 3.0 10.9 1.0 C1A A:HEM295 3.0 10.9 1.0 C4B A:HEM295 3.1 10.6 1.0 C1D A:HEM295 3.1 9.6 1.0 C1B A:HEM295 3.1 11.3 1.0 C4A A:HEM295 3.1 11.2 1.0 CHC A:HEM295 3.4 10.0 1.0 CHA A:HEM295 3.4 10.9 1.0 CHB A:HEM295 3.4 10.3 1.0 CHD A:HEM295 3.5 8.8 1.0 NE1 A:TRP51 4.0 12.3 1.0 NE A:ARG48 4.1 16.0 1.0 ND1 A:HIS175 4.2 11.5 1.0 CG A:HIS175 4.2 11.6 1.0 O A:HOH493 4.2 17.8 1.0 C3C A:HEM295 4.3 8.5 1.0 C3D A:HEM295 4.3 9.3 1.0 C2C A:HEM295 4.3 8.9 1.0 C2A A:HEM295 4.3 11.4 1.0 C3A A:HEM295 4.3 10.3 1.0 C2B A:HEM295 4.3 10.1 1.0 C2D A:HEM295 4.3 10.3 1.0 C3B A:HEM295 4.3 10.9 1.0 CD1 A:TRP51 4.5 11.6 1.0 NH2 A:ARG48 4.6 15.1 1.0 C1 A:LG5401 4.7 10.2 1.0 CZ A:ARG48 4.9 16.8 1.0 CG A:ARG48 4.9 12.2 1.0 CD A:ARG48 5.0 14.1 1.0

R.Brenk, S.W.Vetter, S.E.Boyce, D.B.Goodin, B.K.Shoichet. Probing Molecular Docking in A Charged Model Binding Site. J.Mol.Biol. V. 357 1449 2006.
ISSN: ISSN 0022-2836
PubMed: 16490206
DOI: 10.1016/J.JMB.2006.01.034